3N25

The structure of muscle pyruvate kinase in complex with proline, pyruvate, and Mn2+

3N25 の概要

• エントリーDOI: 10.2210/pdb3n25/pdb
• 分子名称: Pyruvate kinase isozymes M1/M2, PROLINE, MANGANESE (II) ION, ... (9 entities in total)
• 機能のキーワード: pyruvate kinase, glycolysis, allosteric regulation, transferase
• 由来する生物種: Oryctolagus cuniculus (European rabbit,Japanese white rabbit,domestic rabbit,rabbits)
• 細胞内の位置: Cytoplasm : P11974
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 470150.38

構造登録者

Fenton, A.W.,Johnson, T.A.,Holyoak, T. (登録日: 2010-05-17, 公開日: 2010-07-28, 最終更新日: 2023-11-15)

主引用文献

Fenton, A.W.,Johnson, T.A.,Holyoak, T.
The pyruvate kinase model system, a cautionary tale for the use of osmolyte perturbations to support conformational equilibria in allostery.
Protein Sci., 19:1796-1800, 2010

PubMed Abstract: In the study of rabbit muscle pyruvate kinase (M1-PYK), proline has previously been used as an osmolyte in an attempt to determine a role for preexisting conformational equilibria in allosteric regulation. In this context, osmolytes are small molecules assumed to have no direct interaction with the protein. In contrast to proline's proposed role as an osmolyte, the structure of M1PYK-Mn-pyruvate-proline complex reported herein demonstrates that proline binds specifically to the allosteric site of M1-PYK. Therefore, this amino acid is an allosteric effector rather than a benign osmolyte. Other compounds often used as osmolytes (polyethyleneglycol and glycerol) are also present in the structure, suggesting an interaction with the protein that would, in turn, prevent the usefulness of these compounds in the study of this and most likely other proteins. These findings highlight the need to verify that compounds used as osmolytes to perturb preexisting conformational equilibrium do not directly interact with the protein, a consideration not commonly addressed in the past.

PubMed: 20629175
DOI: 10.1002/pro.450

実験手法

X-RAY DIFFRACTION (2.41 Å)